a tool for identifying drug-targetable redox-active disulphides

Dynein assembly factor with WDR repeat domains 1

Intramolecular

Cysteine 159 and cysteine 169

Cysteine 106 and cysteine 116

Cysteine 310 and cysteine 393

Cysteine 285 and cysteine 310

A redox-regulated disulphide may form within Dynein assembly factor with WDR repeat domains 1 between cysteines 159 and 169. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

42

PDB code

Structure name

crystal structure of human oda16

Structure deposition date

2017-04-10

Thiol separation (Å)

9

Half-sphere exposure sum ?

76

Minimum pK_a ?

10

% buried

73

Peptide accession

Residue number A

159

Residue number B

169

Peptide name

Dynein assembly factor with WDR repeat domains 1

Ligandability

Cysteine 159 of Dynein assembly factor with WDR repeat domains 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 169 of Dynein assembly factor with WDR repeat domains 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dynein assembly factor with WDR repeat domains 1 between cysteines 106 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

30

PDB code

Structure name

crystal structure of human oda16

Structure deposition date

2017-04-10

Thiol separation (Å)

9

Half-sphere exposure sum ?

88

Minimum pK_a ?

13

% buried

84

Peptide accession

Residue number A

106

Residue number B

116

Peptide name

Dynein assembly factor with WDR repeat domains 1

Ligandability

Cysteine 106 of Dynein assembly factor with WDR repeat domains 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 116 of Dynein assembly factor with WDR repeat domains 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dynein assembly factor with WDR repeat domains 1 between cysteines 310 and 393. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

25

PDB code

Structure name

crystal structure of human oda16

Structure deposition date

2017-04-10

Thiol separation (Å)

10

Half-sphere exposure sum ?

85

Minimum pK_a ?

12

% buried

100

Peptide accession

Residue number A

310

Residue number B

393

Peptide name

Dynein assembly factor with WDR repeat domains 1

Ligandability

Cysteine 310 of Dynein assembly factor with WDR repeat domains 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 393 of Dynein assembly factor with WDR repeat domains 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dynein assembly factor with WDR repeat domains 1 between cysteines 285 and 310. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

21

PDB code

Structure name

crystal structure of human oda16

Structure deposition date

2017-04-10

Thiol separation (Å)

10

Half-sphere exposure sum ?

94

Minimum pK_a ?

12

% buried

100

Peptide accession

Residue number A

285

Residue number B

310

Peptide name

Dynein assembly factor with WDR repeat domains 1

Ligandability

Cysteine 285 of Dynein assembly factor with WDR repeat domains 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 310 of Dynein assembly factor with WDR repeat domains 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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